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Updated: Jul 16, 2026

Bioluminescence Imaging of NADPH Oxidase Activity in Different Animal Models
Published on: October 22, 2012
NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin
1Department of Biochemistry, University of Geneva, Geneva 4, Switzerland.
Abstract:
Superoxide generation by NADPH oxidase 5 (NOX5) is regulated by Ca(2+) through intramolecular activation of the C-terminal catalytic domain by the EF-hand-containing N-terminal regulatory domain. The C terminus contains a consensus calmodulin-binding domain (CaMBD), which, however, is not the binding site of the N-terminal regulatory domain. Here we show by pull down, cross-linking, fluorimetry and by enzymatic assays, that calmodulin binds to this CaMBD in a Ca(2+)-dependent manner, changes its conformation and increases the Ca(2+) sensitivity of the N terminus-regulated enzymatic activity. This mechanism represents an additional sophistication in the regulation of superoxide production by NOX5.
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